5HUB

High-resolution structure of chorismate mutase from Corynebacterium glutamicum

Summary for 5HUB

• Entry DOI: 10.2210/pdb5hub/pdb
• Descriptor: Chorismate mutase, FORMIC ACID (3 entities in total)
• Functional Keywords: chorismate mutase, shikimate pathway, pericyclic reaction, isomerase
• Biological source: Corynebacterium glutamicum
• Total number of polymer chains: 1
• Total formula weight: 10157.57

Authors

Burschowsky, D.,Heim, J.B.,Thorbjoernsrud, H.V.,Krengel, U. (deposition date: 2016-01-27, release date: 2017-08-02, Last modification date: 2024-01-10)

Primary citation

Burschowsky, D.,Thorbjornsrud, H.V.,Heim, J.B.,Fahrig-Kamarauskaite, J.R.,Wurth-Roderer, K.,Kast, P.,Krengel, U.
Inter-Enzyme Allosteric Regulation of Chorismate Mutase in Corynebacterium glutamicum: Structural Basis of Feedback Activation by Trp.
Biochemistry, 57:557-573, 2018

PubMed Abstract: Corynebacterium glutamicum is widely used for the industrial production of amino acids, nucleotides, and vitamins. The shikimate pathway enzymes DAHP synthase (CgDS, Cg2391) and chorismate mutase (CgCM, Cgl0853) play a key role in the biosynthesis of aromatic compounds. Here we show that CgCM requires the formation of a complex with CgDS to achieve full activity, and that both CgCM and CgDS are feedback regulated by aromatic amino acids binding to CgDS. Kinetic analysis showed that Phe and Tyr inhibit CgCM activity by inter-enzyme allostery, whereas binding of Trp to CgDS strongly activates CgCM. Mechanistic insights were gained from crystal structures of the CgCM homodimer, tetrameric CgDS, and the heterooctameric CgCM-CgDS complex, refined to 1.1, 2.5, and 2.2 Å resolution, respectively. Structural details from the allosteric binding sites reveal that DAHP synthase is recruited as the dominant regulatory platform to control the shikimate pathway, similar to the corresponding enzyme complex from Mycobacterium tuberculosis.

PubMed: 29178787
DOI: 10.1021/acs.biochem.7b01018

Experimental method

X-RAY DIFFRACTION (1.06 Å)